Structure of PDB 6vfx Chain A

Receptor sequence
>6vfxA (length=340) Species: 487 (Neisseria meningitidis) [Search protein sequence]
KLPTPAEIVANLNDHVIGQEQAKKALAVSVYNHYKRLRHPKAGANVELSK
SNILLIGPTGSGKTLLAQSLARKLDVPFVMADATTLTEAGYVGEDVEQII
TKLLGKCDFDVEKAQRGIVYIDQIDKISRKSDNPSITRDVSGEGVQQALL
KLIEGTVASVPPQGGEFINVDTTNILFICGGAFAGLEKVIRQRTEKGGIG
FGASVHNADITKLFGIVEPEDLIKFGLIPELIGRLPVIATLEILDEDALI
NILTEPKNALVKQYQALFGMENVELEFEEGALRSIARQAMERKTGARGLR
SIVERCLLDTMYRLPDLKGLKKVVVGKAVIEEGREPELVF
3D structure
PDB6vfx A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery.
ChainA
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide A N195 P196 S197 I198 T199 N133 P134 S135 I136 T137
BS02 ATP A V78 I79 T121 G122 S123 G124 K125 T126 L127 I324 A368 R369 V16 I17 T59 G60 S61 G62 K63 T64 L65 I252 A296 R297
BS03 MG A T126 D184 T64 D122
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0051301 cell division
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0009376 HslUV protease complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6vfx, PDBe:6vfx, PDBj:6vfx
PDBsum6vfx
PubMed31916936
UniProtQ9JYY3|CLPX_NEIMB ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)

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